scholarly journals Cysteine containing dipeptides show a metal specificity that matches the composition of seawater

2016 ◽  
Vol 18 (30) ◽  
pp. 20104-20108 ◽  
Author(s):  
Luca Belmonte ◽  
Daniele Rossetto ◽  
Michele Forlin ◽  
Simone Scintilla ◽  
Claudia Bonfio ◽  
...  
Keyword(s):  
Metal Specificity

Cysteine containing dipeptide metal affinities do not follow the Irving–Williams series but rather follow the concentration trends found in seawater.

Distinct Metal Environment in Fe-Substituted Manganese Superoxide Dismutase Provides a Structural Basis of Metal Specificity

1998 ◽  
Vol 120 (37) ◽  
pp. 9684-9685 ◽  
Author(s):  
Ross A. Edward ◽  
Mei M. Whittaker ◽  
James W. Whittaker ◽  
Geoffrey B. Jameson ◽  
Edward N. Baker
Keyword(s):  
Superoxide Dismutase ◽  
Manganese Superoxide Dismutase ◽  
Structural Basis ◽  
Metal Specificity ◽  
Manganese Superoxide

Engineering new metal specificity in EF-hand peptides

2003 ◽  
Vol 8 (3) ◽  
pp. 334-340 ◽  
Author(s):  
Loïc Le Clainche ◽  
Gabriel Plancque ◽  
Badia Amekraz ◽  
Christophe Moulin ◽  
Catherine Pradines-Lecomte ◽  
...  
Keyword(s):  
Metal Specificity ◽  
Ef Hand

scholarly journals Functional Determinants of Metal Ion Transport and Selectivity in Paralogous Cation Diffusion Facilitator Transporters CzcD and MntE in Streptococcus pneumoniae

2016 ◽  
Vol 198 (7) ◽  
pp. 1066-1076 ◽  
Author(s):  
Julia E. Martin ◽  
David P. Giedroc
Keyword(s):  
Streptococcus Pneumoniae ◽  
Metal Ion ◽  
Transmembrane Domain ◽  
Divalent Metal ◽  
Cation Diffusion ◽  
Metal Specificity ◽  
Cation Diffusion Facilitator ◽  
Content Type ◽  
Metal Selectivity ◽  
A Site

ABSTRACTCation diffusion facilitators (CDFs) are a large family of divalent metal transporters that collectively possess broad metal specificity and contribute to intracellular metal homeostasis and virulence in bacterial pathogens.Streptococcus pneumoniaeexpresses two homologous CDF efflux transporters, MntE and CzcD. Cells lackingmntEorczcDare sensitive to manganese (Mn) or zinc (Zn) toxicity, respectively, and specifically accumulate Mn or Zn, respectively, thus suggesting that MntE selectively transports Mn, while CzcD transports Zn. Here, we probe the origin of this metal specificity using a phenotypic growth analysis of pneumococcal variants. Structural homology toEscherichia coliYiiP predicts that both MntE and CzcD are dimeric and each protomer harbors four pairs of conserved metal-binding sites, termed the A site, the B site, and the C1/C2 binuclear site. We find that single amino acid mutations within both the transmembrane domain A site and the B site in both CDFs result in a cellular metal sensitivity similar to that of the corresponding null mutants. However, multiple mutations in the predicted cytoplasmic C1/C2 cluster of MntE have no impact on cellular Mn resistance, in contrast to the analogous substitutions in CzcD, which do have on impact on cellular Zn resistance. Deletion of the MntE-specific C-terminal tail, present only in Mn-specific bacterial CDFs, resulted in only a modest growth phenotype. Further analysis of MntE-CzcD functional chimeric transporters showed that Asn and Asp in theND-DD A-site motif of MntE and the most N-terminal His in theHD-HD site A of CzcD (the specified amino acids are underlined) play key roles in transporter metal selectivity.IMPORTANCECation diffusion facilitator (CDF) proteins are divalent metal ion transporters that are conserved in organisms ranging from bacteria to humans and that play important roles in cellular physiology, from metal homeostasis and resistance to type I diabetes in vertebrates. The respiratory pathogenStreptococcus pneumoniaeexpresses two metal CDF transporters, CzcD and MntE. How CDFs achieve metal selectivity is unclear. We show here that CzcD and MntE are true paralogs, as CzcD transports zinc, while MntE selectively transports manganese. Through the use of an extensive collection of pneumococcal variants, we show that a primary determinant for metal selectivity is the A site within the transmembrane domain. This extends our understanding of how CDFs discriminate among transition metals.

Efficient preparation and metal specificity of the regulatory protein TroR from the human pathogen Treponema pallidum

Metallomics ◽  
2013 ◽  
Vol 5 (10) ◽  
pp. 1448 ◽  
Author(s):  
Yi Liu ◽  
Wei Li ◽  
Yaozhu Wei ◽  
Yindi Jiang ◽  
Xiangshi Tan
Keyword(s):  
Regulatory Protein ◽  
Treponema Pallidum ◽  
Human Pathogen ◽  
Metal Specificity

scholarly journals Structural Basis of the Metal Specificity for Nickel Regulatory Protein NikR†,‡

Biochemistry ◽  
2008 ◽  
Vol 47 (7) ◽  
pp. 1938-1946 ◽  
Author(s):  
Christine M. Phillips ◽  
Eric R. Schreiter ◽  
Yayi Guo ◽  
Sheila C. Wang ◽  
Deborah B. Zamble ◽  
...  
Keyword(s):  
Regulatory Protein ◽  
Structural Basis ◽  
Metal Specificity
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